Expression, purification, crystallization and preliminary X-ray crystallographic analysis of Enpp6

Acta Crystallogr F Struct Biol Commun. 2014 Jun;70(Pt 6):794-9. doi: 10.1107/S2053230X14008929. Epub 2014 May 24.

Abstract

Enpp (ectonucleotide phosphodiesterase/pyrophosphatase) 6 is a membrane-bound glycoprotein that hydrolyzes choline-containing compounds such as lysophosphatidylcholine and glycerophosphorylcholine, and presumably participates in choline metabolism. The catalytic domain of mouse Enpp6 was expressed in HEK293T cells, purified using the TARGET tag/P20.1-Sepharose system and crystallized. An X-ray diffraction data set was collected to 1.8 Å resolution. The crystal belonged to space group P1, with unit-cell parameters a=63.7, b=68.8, c=69.7 Å, α=60.6, β=87.0, γ=68.1°. Assuming the presence of two protein molecules per asymmetric unit, the solvent content was estimated to be 49.5%.

Keywords: Enpp6; N-glycosylation; choline.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Crystallization
  • Crystallography, X-Ray
  • Molecular Sequence Data
  • Phosphoric Diester Hydrolases / chemistry*
  • Sequence Homology, Amino Acid

Substances

  • Phosphoric Diester Hydrolases
  • ENPP6 protein, human